4R4Y
Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003948 | molecular_function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity |
A | 0004067 | molecular_function | asparaginase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006508 | biological_process | proteolysis |
A | 0006517 | biological_process | protein deglycosylation |
A | 0008233 | molecular_function | peptidase activity |
A | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0042597 | cellular_component | periplasmic space |
B | 0003948 | molecular_function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity |
B | 0004067 | molecular_function | asparaginase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006508 | biological_process | proteolysis |
B | 0006517 | biological_process | protein deglycosylation |
B | 0008233 | molecular_function | peptidase activity |
B | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SD4 A 301 |
Chain | Residue |
A | HIS150 |
A | HOH436 |
A | HOH437 |
A | ASP151 |
A | THR152 |
A | ASP172 |
A | ARG180 |
A | ASP183 |
A | THR203 |
A | GLY204 |
A | GLY206 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:10490104, ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597, ECO:0000269|PubMed:9685368 |
Chain | Residue | Details |
A | THR152 | |
B | THR152 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG180 | |
A | THR203 | |
B | ARG180 | |
B | THR203 |